Fibrinogen integrins interactions with

The extracellular domains of integrins interact with a variety of profeins of the extracellular matrix. These include fibronectin, fibrinogen, vifronecfin, collagen, and entacfin. Other large cell surface adhesins include laminin and osteopontin (Chapfer 8), thrombospondin, von Willebrand factor, and related proteins. These adhesins appear to depend upon the sequence Arg-Gly-Asp (RGD), which binds nonco-valently to integrins, which act as cell-surface receptors. See also Chapter 12, Section C,9. 

The next step in neutrophil extravasation is inhibited by the Extracellular adherence protein (Eap) of S. aureus. Eap inhibits direct interactions with the host adhesive proteins intercellular adhesion molecule 1 (ICAM-1), fibrinogen or vitronectin, Eap disrupted beta(2)-integrin and urokinase receptor mediated leukocyte adhesion in vitro. In a bacterial peritonitis mouse model, Eap-expressing S. aureus (or isolated Eap) elicited less neutrophil influx as compared to an Eap-negative strain. - Further Eap protects in an ICAM-1 dependent experimental autoimmune encephalomyelitis (EAE) in mice, indicating that Eap could possibly represent a treatment... 

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